4ijr | pdb_00004ijr

Crystal structure of Saccharomyces cerevisiae arabinose dehydrogenase Ara1 complexed with NADPH

spinqualitylabelsall models 4ijr, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ijr is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ARA1_YEAST Catalyzes the oxidation of D-arabinose, L-xylose, L-fucose and L-galactose in the presence of NADP(+). Publication Abstract from PubMed The primary role of yeast Ara1, previously mis-annotated as a D-arabinose dehydrogenase, is to catalyze the reduction of a variety of toxic alpha,beta-dicarbonyl compounds using NADPH as a cofactor at physiological pH levels. Here, crystal structures of Ara1 in apo and NADPH-complexed forms are presented at 2.10 and 2.00 A resolution, respectively. Ara1 exists as a homodimer, each subunit of which adopts an (alpha/beta)8-barrel structure and has a highly conserved cofactor-binding pocket. Structural comparison revealed that induced fit upon NADPH binding yielded an intact active-site pocket that recognizes the substrate. Moreover, the crystal structures combined with computational simulation defined an open substrate-binding site to accommodate various substrates that possess a dicarbonyl group. Structures of Saccharomyces cerevisiaeD-arabinose dehydrogenase Ara1 and its complex with NADPH: implications for cofactor-assisted substrate recognition.,Hu XQ, Guo PC, Ma JD, Li WF Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1190-5. doi:, 10.1107/S1744309113026857. Epub 2013 Oct 26. PMID:24192347 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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